The effects of protein charge patterning on complex coacervation

Soft Matter ◽  
2021 ◽  
Author(s):  
Nicholas A. Zervoudis ◽  
Allie C. Obermeyer
Keyword(s):  
Globular Proteins ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge

Charge patterned polypeptides modulate the complex coacervation of globular proteins with polymers. These protein coacervates have applications in protein encapsulation and delivery and in determining the function of biomolecular condensates.

The Effects of Protein Charge Patterning on Complex Coacervation

2021 ◽  
Author(s):  
Nicholas Zervoudis ◽  
Allie Obermeyer
Keyword(s):  
Phase Boundary ◽  
Phase Behavior ◽  
Predictive Models ◽  
Phase Portraits ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge ◽  
Polypeptide Sequence ◽  
The Impact ◽  
Coacervate Phase

The complex coacervation of proteins with other macromolecules has applications in protein encapsulation and delivery and for determining the function of cellular coacervates. Theoretical or empirical predictions for protein coacervates would enable the design of these coacervates with tunable and predictable structure-function relationships; unfortunately, no such theories exist. To help establish predictive models, the impact of protein-specific parameters on complex coacervation were probed in this study. The complex coacervation of sequence-specific, polypeptide-tagged, GFP variants and a strong synthetic polyelectrolyte was used to evaluate the effects of protein charge patterning on phase behavior. Phase portraits for the protein coacervates demonstrated that charge patterning dictates the protein’s binodal phase boundary. Protein concentrations over 100 mg mL<sup>-1</sup> were achieved in the coacervate phase, with concentrations dependent on the polypeptide sequence. In addition to shifting the binodal phase boundary, polypeptide charge patterning provided entropic advantages over isotropically patterned proteins. Together, these results show that modest changes of only a few amino acids alter the coacervation thermodynamics and can be used to tune the phase behavior of polypeptides or proteins of interest.

scholarly journals The Effects of Protein Charge Patterning on Complex Coacervation

2021 ◽  
Author(s):  
Nicholas Zervoudis ◽  
Allie Obermeyer
Keyword(s):  
Phase Boundary ◽  
Phase Behavior ◽  
Predictive Models ◽  
Phase Portraits ◽  
Complex Coacervation ◽  
Protein Encapsulation ◽  
Protein Charge ◽  
Polypeptide Sequence ◽  
The Impact ◽  
Coacervate Phase

The complex coacervation of proteins with other macromolecules has applications in protein encapsulation and delivery and for determining the function of cellular coacervates. Theoretical or empirical predictions for protein coacervates would enable the design of these coacervates with tunable and predictable structure-function relationships; unfortunately, no such theories exist. To help establish predictive models, the impact of protein-specific parameters on complex coacervation were probed in this study. The complex coacervation of sequence-specific, polypeptide-tagged, GFP variants and a strong synthetic polyelectrolyte was used to evaluate the effects of protein charge patterning on phase behavior. Phase portraits for the protein coacervates demonstrated that charge patterning dictates the protein’s binodal phase boundary. Protein concentrations over 100 mg mL<sup>-1</sup> were achieved in the coacervate phase, with concentrations dependent on the polypeptide sequence. In addition to shifting the binodal phase boundary, polypeptide charge patterning provided entropic advantages over isotropically patterned proteins. Together, these results show that modest changes of only a few amino acids alter the coacervation thermodynamics and can be used to tune the phase behavior of polypeptides or proteins of interest.

scholarly journals Ionic polypeptide tags for protein phase separation

2019 ◽  
Vol 10 (9) ◽  
pp. 2700-2707 ◽  
Author(s):  
Rachel A. Kapelner ◽  
Allie C. Obermeyer
Keyword(s):  
Phase Separation ◽  
Globular Proteins ◽  
Complex Coacervation ◽  
Protein Activity ◽  
Physiological Conditions

Short ionic polypeptide tags were demonstrated to drive complex coacervation of globular proteins at physiological conditions while maintaining protein activity.

The role of protein charge in protein-lipid interactions. pH-Dependent changes of the electrophoretic mobility of liposomes through adsorption of water-soluble, globular proteins

Biochemistry ◽  
1993 ◽  
Vol 32 (17) ◽  
pp. 4641-4649 ◽  
Author(s):  
Joep J. Bergers ◽  
Monique H. Vingerhoeds ◽  
Louis van Bloois ◽  
James N. Herron ◽  
Lambert H. M. Janssen ◽  
...  
Keyword(s):  
Electrophoretic Mobility ◽  
Globular Proteins ◽  
Water Soluble ◽  
Protein Charge ◽  
Lipid Interactions ◽  
Adsorption Of Water ◽  
Ph Dependent

Protein Encapsulation via Polypeptide Complex Coacervation

2014 ◽  
Vol 3 (10) ◽  
pp. 1088-1091 ◽  
Author(s):  
Katie A. Black ◽  
Dimitrios Priftis ◽  
Sarah L. Perry ◽  
Jeremy Yip ◽  
William Y. Byun ◽  
...  
Keyword(s):  
Complex Coacervation ◽  
Protein Encapsulation

Albumins as Embedding Media for Electron Microscopy

1969 ◽  
Vol 27 ◽  
pp. 422-423 ◽  
Author(s):  
J. L. Farrant ◽  
J. D. McLean
Keyword(s):  
Electron Microscopy ◽  
Electron Microscope ◽  
High Temperature ◽  
Biological Material ◽  
Globular Proteins ◽  
The Past ◽  
Antibody Staining ◽  
Thin Sectioning ◽  
Embedding Medium

For electron microscope techniques such as ferritin-labeled antibody staining it would be advantageous to have available a simple means of thin sectioning biological material without subjecting it to lipid solvents, impregnation with plastic monomers and their subsequent polymerization. With this aim in view we have re-examined the use of protein as an embedding medium. Gelatin which has been used in the past is not very satisfactory both because of its fibrous nature and the high temperature necessary to keep its solutions fluid. We have found that globular proteins such as the serum and egg albumins can be cross-linked so as to yield blocks which are suitable for ultrathin sectioning.

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